In this paper, we recombine half-barrel-sized segments of two hyperthermophile endoglucanases (a cellulose and a beta-glucosidase) into ‘chimeras’ in different ways and show interesting, and diverse, effects of doing so. With some tendency to multimerize and form soluble aggregates, the resultant protein-engineered variants display interesting levels and combinations of cellulase and/or beta-glucosidase activities, or no detectable activity, depending on the nature of the engineering performed. Of course, the two endoglucanases in this case were selected (based on a detailed pre-examination of structural characteristics and parameters) for the experiment to be likely to fold, and to function. It is not as if we are suggesting that any two half-barrels can be randomly recombined; merely that this is a technology demonstration to show that it is possible to make such chimeras if the structural principles of such protein engineering (explained in the paper) are adhered to.

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